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P13843 (FUS_HRSV1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 5, 2011. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Fusion glycoprotein F0

Cleaved into the following 2 chains:

  1. Fusion glycoprotein F2
  2. Fusion glycoprotein F1
Gene names
Name:F
OrganismHuman respiratory syncytial virus B (strain 18537)
Taxonomic identifier11251 [NCBI]
Taxonomic lineageViruses › ssRNA negative-strand viruses › Mononegavirales › Paramyxoviridae › Pneumovirinae › Pneumovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length574 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with HN at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis By similarity.

Subunit structure

Homotrimer of disulfide-linked F1-F2 By similarity. Interacts with glycoprotein G. Interacts with host RHOA; this interaction facilitates virus-induced syncytium formation By similarity.

Subcellular location

Virion membrane; Single-pass type I membrane protein By similarity. Host cell membrane; Single-pass membrane protein By similarity.

Post-translational modification

The inactive precursor F0 is glycosylated and proteolytically cleaved into F1 and F2 to be functionally active. The cleavage is mediated by cellular proteases during the transport and maturation of the polypeptide By similarity.

Sequence similarities

Belongs to the paramyxoviruses fusion glycoprotein family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 574552Fusion glycoprotein F0
PRO_0000039237
Chain23 – 136114Fusion glycoprotein F2
PRO_0000039238
Chain137 – 574438Fusion glycoprotein F1
PRO_0000039239

Regions

Topological domain27 – 529503Extracellular By similarity
Transmembrane530 – 55021Helical; Potential
Topological domain551 – 57424Cytoplasmic By similarity
Region137 – 15721Fusion peptide By similarity
Coiled coil155 – 18329 Potential
Coiled coil491 – 51626 Potential

Sites

Site136 – 1372Cleavage; by host By similarity

Amino acid modifications

Lipidation5501S-palmitoyl cysteine; by host By similarity
Glycosylation271N-linked (GlcNAc...); by host Potential
Glycosylation701N-linked (GlcNAc...); by host Potential
Glycosylation1161N-linked (GlcNAc...); by host Potential
Glycosylation1201N-linked (GlcNAc...); by host Potential
Glycosylation1261N-linked (GlcNAc...); by host Potential
Glycosylation5001N-linked (GlcNAc...); by host Potential
Disulfide bond69 ↔ 212Interchain (between F2 and F1 chains) By similarity
Disulfide bond358 ↔ 367 By similarity
Disulfide bond382 ↔ 393 By similarity

Sequences

Sequence LengthMass (Da)Tools
P13843 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 5B48D47402395816

FASTA57463,688
        10         20         30         40         50         60 
MELLIHRSSA IFLTLAVNAL YLTSSQNITE EFYQSTCSAV SRGYFSALRT GWYTSVITIE 

        70         80         90        100        110        120 
LSNIKETKCN GTDTKVKLIK QELDKYKNAV TELQLLMQNT PAANNRARRE APQYMNYTIN 

       130        140        150        160        170        180 
TTKNLNVSIS KKRKRRFLGF LLGVGSAIAS GIAVSKVLHL EGEVNKIKNA LLSTNKAVVS 

       190        200        210        220        230        240 
LSNGVSVLTS KVLDLKNYIN NRLLPIVNQQ SCRISNIETV IEFQQMNSRL LEITREFSVN 

       250        260        270        280        290        300 
AGVTTPLSTY MLTNSELLSL INDMPITNDQ KKLMSSNVQI VRQQSYSIMS IIKEEVLAYV 

       310        320        330        340        350        360 
VQLPIYGVID TPCWKLHTSP LCTTNIKEGS NICLTRTDRG WYCDNAGSVS FFPQADTCKV 

       370        380        390        400        410        420 
QSNRVFCDTM NSLTLPSEVS LCNTDIFNSK YDCKIMTSKT DISSSVITSL GAIVSCYGKT 

       430        440        450        460        470        480 
KCTASNKNRG IIKTFSNGCD YVSNKGVDTV SVGNTLYYVN KLEGKNLYVK GEPIINYYDP 

       490        500        510        520        530        540 
LVFPSDEFDA SISQVNEKIN QSLAFIRRSD ELLHNVNTGK STTNIMITTI IIVIIVVLLS 

       550        560        570 
LIAIGLLLYC KAKNTPVTLS KDQLSGINNI AFSK

« Hide

References

[1]"The fusion glycoproteins of human respiratory syncytial virus of subgroups A and B: sequence conservation provides a structural basis for antigenic relatedness."
Johnson P.R., Collins P.L.
J. Gen. Virol. 69:2623-2628(1988) [PubMed: 3171553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D00334 Genomic RNA. Translation: BAA00240.1.
PIRVGNZHB. A28929.

3D structure databases

ProteinModelPortalP13843.
SMRP13843. Positions 158-207, 477-516.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000776. Fusion_gly.
[Graphical view]
PfamPF00523. Fusion_gly. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB00110. Palivizumab.

Entry information

Entry nameFUS_HRSV1
AccessionPrimary (citable) accession number: P13843
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 5, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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